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- W1980996961 abstract "Class A and class B NAD(H):NADP(H) coenzyme-dependent dehydrogenases distinguish between the diastereotopic hydrogens pro-R and pro-S at position 4 of the cofactor. We investigated the stereochemistry of hydride transfer in reactions catalyzed by an unusual thermophilic, zinc-containing, NADP-linked enzyme Thermoanaerobium brockii alcohol dehydrogenase (TBAD). Using proton NMK spectroscopy of monodeuterated alcohols and coenzymes we found that TBAD is a class A enzyme that transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over (a) a broad range of temperatures up to 70° C. (b) different concentrations of the coenzyme (catalytic or stoichiometric) and (c) a wide scope of substrates. Although NAD + is not an effective coenzyme for TBAD, NADP + and its synthetic analogs, 3-acetqlpyridine-ADP + and thio-NADP +, can be used successfully." @default.
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- W1980996961 date "2009-01-12" @default.
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- W1980996961 title "Stereospecificity of hydrogen transfer by the NADP-linked alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii" @default.
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- W1980996961 doi "https://doi.org/10.1111/j.1399-3011.1993.tb00159.x" @default.
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